Ca²⁺-based allosteric switches and shape shifting in RGLG1 VWA domain.

ABSTRACT: RGLG1 is an E3 ubiquitin ligase in Arabidopsis thaliana that participates in ABA signaling and regulates apical dominance. Here, we present crystal structures of RGLG1 VWA domain, revealing two novel calcium ions binding sites (NCBS1 and NCBS2). Furthermore, the structures with guided mutagenesis in NCBS1 prove that Ca²⁺ ions play important roles in controlling conformational change of VWA, which is stabilized in open state with Ca²⁺ bound and converted to closed state after Ca²⁺ removal. This allosteric regulation mechanism is distinct from the ever reported one involving the C-terminal helix in integrin α and β I domains. The mutation of a key residue in NCBS2 do not abolish its Ca²⁺-binding potential, with no conformational change. MD s

SUBMITTER: Wang Q 

PROVIDER: S-EPMC7155146 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature